ID A0A163K3U2_ABSGL Unreviewed; 604 AA.
AC A0A163K3U2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=SRP54-type proteins GTP-binding domain-containing protein {ECO:0000259|PROSITE:PS00300};
GN Name=ABSGL_11220.1 scaffold 12295 {ECO:0000313|EMBL:SAM05345.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM05345.1};
RN [1] {ECO:0000313|EMBL:SAM05345.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM05345.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family.
CC {ECO:0000256|ARBA:ARBA00008531}.
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DR EMBL; LT554468; SAM05345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163K3U2; -.
DR STRING; 4829.A0A163K3U2; -.
DR InParanoid; A0A163K3U2; -.
DR OMA; HLGWIDK; -.
DR OrthoDB; 5475029at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0005785; C:signal recognition particle receptor complex; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005047; F:signal recognition particle binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd14826; SR_alpha_SRX; 1.
DR CDD; cd17876; SRalpha_C; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007222; Sig_recog_particle_rcpt_asu_N.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43134:SF1; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR Pfam; PF04086; SRP-alpha_N; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; Domain of the SRP/SRP receptor G-proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT DOMAIN 582..595
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 128..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 66583 MW; 9051603BD001562F CRC64;
MLDLFTILNK GGLVLWKHAY TSLTGSPVEG LIKNILIEER SGTDIYIKDT YALKWTFANE
LDLVFVVAYQ KILQLSYIDE LLETIKRLFI ETYKDTVVTD QGIHGDYSDF DAVFSKVLVS
LEQKHSSNRA RAPRKFENTK KFETTLKGSQ APVSQSTASN TKVDNDEITK NIKALKLQGS
PRGKGGRKQP PSRTTSSTAS PSTEKKKSQK QMRVWDGQIA KGEMEALDYS GGGGDDTVDE
ALIKAQHLDA AKLGTKNNQG IYEVQDVDVP EDDEDEDYDF GDDDEDDNDG SNKGGIFSFF
KSMTGQREMT EETLDPVLAT MKDSMIDKNV GKEIADRLCE SVKSSLLGKK LGSFERVSAV
VRTSMESALK RILTPKTSLD ILRDIEQAKS EKRPYVITFI GVNGVGKSTN LSKVCFWLLQ
NNVKVLIAAC DTFRSGAVEQ LRVHARNLRA LQTSGGGVVE LFERGYGKDS AGIAKDAIAY
AGANNFDVVL IDTAGRMQDN EPLMRALSKL VSVNNPDKII FVGEALVGNE AVDQLTKFNN
ALKDFSGLQN PRHIDGMILT KFDTIDDKVG AALTMTYITG QPIYFVGCGQ TYRKFDIITF
GTAS
//
